CN101674846B - ErbB3抗体及其用途 - Google Patents
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- CN101674846B CN101674846B CN200880009633.1A CN200880009633A CN101674846B CN 101674846 B CN101674846 B CN 101674846B CN 200880009633 A CN200880009633 A CN 200880009633A CN 101674846 B CN101674846 B CN 101674846B
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US90190407P | 2007-02-16 | 2007-02-16 | |
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US979608P | 2008-01-02 | 2008-01-02 | |
US61/009,796 | 2008-01-02 | ||
PCT/US2008/002119 WO2008100624A2 (fr) | 2007-02-16 | 2008-02-15 | Anticorps contre erbb3 et leur utilisation |
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Families Citing this family (184)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
AUPQ105799A0 (en) | 1999-06-18 | 1999-07-08 | Victor Chang Cardiac Research Institute, The | Cell growth inhibition |
CA2480099C (fr) | 2002-03-26 | 2019-01-08 | Zensun (Shanghai) Sci-Tech. Ltd. | Procedes fondes sur l'utilisation de erbb3 et compositions associees de traitement des neoplasmes |
US20040067532A1 (en) | 2002-08-12 | 2004-04-08 | Genetastix Corporation | High throughput generation and affinity maturation of humanized antibody |
US8505468B2 (en) * | 2002-11-19 | 2013-08-13 | Sharp Kabushiki Kaisha | Substrate accommodating tray |
KR101462819B1 (ko) | 2004-05-03 | 2014-11-21 | 헤르메스 바이오사이언스, 인코포레이티드 | 약물 전달에 유용한 리포좀 |
EP2647388A1 (fr) * | 2007-02-16 | 2013-10-09 | Merrimack Pharmaceuticals, Inc. | Anticorps dirigés contre l'ERBB3 et leurs utilisations |
CA2680237C (fr) | 2007-03-27 | 2018-11-06 | Sea Lane Biotechnologies, Llc | Constructions et bibliotheques comprenant des sequences de chaines legeres de substitution d'anticorps |
US8877688B2 (en) | 2007-09-14 | 2014-11-04 | Adimab, Llc | Rationally designed, synthetic antibody libraries and uses therefor |
EP3124497B1 (fr) | 2007-09-14 | 2020-04-15 | Adimab, LLC | Bibliothèques d'anticorps synthétiques conçus de façon rationnelle et leurs utilisations |
US9266967B2 (en) | 2007-12-21 | 2016-02-23 | Hoffmann-La Roche, Inc. | Bivalent, bispecific antibodies |
US20090162359A1 (en) | 2007-12-21 | 2009-06-25 | Christian Klein | Bivalent, bispecific antibodies |
BRPI0910482A2 (pt) | 2008-04-29 | 2019-09-24 | Abbott Lab | imunoglobinas de domínio variável duplo e usos das mesmas |
NZ589436A (en) | 2008-06-03 | 2012-12-21 | Abbott Lab | Dual variable domain immunoglobulins and uses thereof |
JP2011523853A (ja) | 2008-06-03 | 2011-08-25 | アボット・ラボラトリーズ | 二重可変ドメイン免疫グロブリン及びその使用 |
JP5674654B2 (ja) | 2008-07-08 | 2015-02-25 | アッヴィ・インコーポレイテッド | プロスタグランジンe2二重可変ドメイン免疫グロブリンおよびその使用 |
PE20120015A1 (es) * | 2008-08-15 | 2012-01-26 | Merrimack Pharmaceuticals Inc | Metodos y sistemas para predecir la respuesta de las celulas tumorales a un agente terapeutico |
SG10201402742YA (en) | 2009-03-20 | 2014-08-28 | Genentech Inc | Bispecific anti-her antibodies |
KR101431318B1 (ko) | 2009-04-02 | 2014-08-20 | 로슈 글리카트 아게 | 전장 항체 및 단일쇄 fab 단편을 포함하는 다중특이성 항체 |
CN102378768A (zh) * | 2009-04-07 | 2012-03-14 | 罗氏格黎卡特股份公司 | 双特异性抗-ErbB-3/抗-c-Met抗体 |
SG175078A1 (en) * | 2009-04-07 | 2011-11-28 | Roche Glycart Ag | Bispecific anti-erbb-1/anti-c-met antibodies |
PL2417156T3 (pl) * | 2009-04-07 | 2015-07-31 | Roche Glycart Ag | Trójwartościowe, bispecyficzne przeciwciała |
AU2010249046A1 (en) | 2009-05-13 | 2011-12-01 | Sea Lane Biotechnologies, Llc | Neutralizing molecules to influenza viruses |
US9676845B2 (en) | 2009-06-16 | 2017-06-13 | Hoffmann-La Roche, Inc. | Bispecific antigen binding proteins |
CA2771744A1 (fr) * | 2009-08-21 | 2011-02-24 | Merrimack Pharmaceuticals, Inc. | Anticorps contre l'ectodomaine de erbb3 et leurs utilisations |
UY32870A (es) | 2009-09-01 | 2011-02-28 | Abbott Lab | Inmunoglobulinas con dominio variable dual y usos de las mismas |
SG10201408401RA (en) | 2009-09-16 | 2015-01-29 | Genentech Inc | Coiled coil and/or tether containing protein complexes and uses thereof |
WO2011044311A2 (fr) * | 2009-10-09 | 2011-04-14 | Merck Sharp & Dohme Corp. | Génération, caractérisation et utilisations d'anticorps anti-her3 |
AU2010306774A1 (en) * | 2009-10-14 | 2012-05-03 | Merrimack Pharmaceuticals, Inc. | Bispecific binding agents targeting IGF-1R and ErbB3 signalling and uses thereof |
BR112012008833A2 (pt) | 2009-10-15 | 2015-09-08 | Abbott Lab | imunoglobulinas de dominio variavel duplo e usos das mesmas |
UY32979A (es) | 2009-10-28 | 2011-02-28 | Abbott Lab | Inmunoglobulinas con dominio variable dual y usos de las mismas |
JP5960598B2 (ja) * | 2009-11-04 | 2016-08-02 | アフィボディ・アーベー | Her3結合ポリペプチド |
DK2719708T3 (da) * | 2009-11-13 | 2018-01-29 | Daiichi Sankyo Europe Gmbh | Materiale og fremgangsmåder til behandling eller forebyggelse af her-3-relaterede sygdomme |
WO2011060380A1 (fr) * | 2009-11-14 | 2011-05-19 | The Regents Of The University Of California | L'état de mutation de pik3ca et l'expression de sash1 prédisent la synergie entre le lapatinib et un inhibiteur d'akt dans le cancer du sein her2 positif |
NZ600262A (en) | 2009-12-22 | 2013-06-28 | Roche Glycart Ag | Anti-her3 antibodies and uses thereof |
KR101913440B1 (ko) | 2010-03-02 | 2018-10-30 | 교와 핫꼬 기린 가부시키가이샤 | 개변 항체 조성물 |
DK2544680T3 (en) | 2010-03-11 | 2015-04-27 | Merrimack Pharmaceuticals Inc | USE OF ErbB3 INHIBITORS IN TREATMENT OF TRIPLE-NEGATIVE BREAST CANCER |
AR080793A1 (es) | 2010-03-26 | 2012-05-09 | Roche Glycart Ag | Anticuerpos biespecificos |
BR112012025730B1 (pt) * | 2010-04-09 | 2020-12-08 | Aveo Pharmaceuticals, Inc | anticorpo isolado que se liga ao erbb3 humano, seus usos, seu processo de produção e vetor de expressão |
US20120010388A1 (en) * | 2010-04-16 | 2012-01-12 | Gottfried Himmler | LeY SPECIFIC BIOTHERAPEUTIC |
MX2012012441A (es) | 2010-05-04 | 2013-02-26 | Merrimack Pharmaceuticals Inc | Anticuerpos contra el receptor del factor de crecimiento epidermico (egfr) y usos de los mismos. |
EP3546483A1 (fr) * | 2010-05-20 | 2019-10-02 | Ablynx N.V. | Matériaux biologiques associés à her3 |
AU2011276285A1 (en) | 2010-07-06 | 2013-01-24 | Aveo Pharmaceuticals, Inc. | Anti-RON antibodies |
UY33498A (es) | 2010-07-09 | 2013-01-03 | Sanofi Aventis | Combinaciones de inhibidores de quinasas para el tratamiento de cancer |
US8735546B2 (en) | 2010-08-03 | 2014-05-27 | Abbvie Inc. | Dual variable domain immunoglobulins and uses thereof |
WO2012019024A2 (fr) * | 2010-08-04 | 2012-02-09 | Immunogen, Inc. | Molécules se liant à her3 et leurs immunoconjugués |
DK2606070T3 (en) | 2010-08-20 | 2017-03-27 | Novartis Ag | Antibodies for the epidermal growth factor receptor 3 (HER3) |
JP5758004B2 (ja) | 2010-08-24 | 2015-08-05 | エフ.ホフマン−ラ ロシュ アーゲーF. Hoffmann−La Roche Aktiengesellschaft | ジスルフィドによって安定化されたFv断片を含む二重特異性抗体 |
CA2809433A1 (fr) | 2010-08-26 | 2012-03-01 | Abbvie Inc. | Immunoglobulines a deux domaines variables et leurs utilisations |
TW201302793A (zh) * | 2010-09-03 | 2013-01-16 | Glaxo Group Ltd | 新穎之抗原結合蛋白 |
EP2630160B1 (fr) * | 2010-10-18 | 2016-11-09 | MediaPharma S.r.l. | Anticorps se liant à erbb3 |
DK2635604T3 (en) * | 2010-11-01 | 2017-02-27 | Symphogen As | PAN-HER-ANTIBODY COMPOSITION |
US9155802B2 (en) | 2010-11-01 | 2015-10-13 | Symphogen A/S | Pan-HER antibody composition |
ITRM20100577A1 (it) * | 2010-11-02 | 2012-05-03 | Takis Srl | Immunoterapia contro il recettore erbb-3 |
EP2648738A2 (fr) | 2010-12-06 | 2013-10-16 | Merrimack Pharmaceuticals, Inc. | Détermination de la dose et administration pour la prévention de la cardiotoxicité dans le traitement par immunoliposomes ciblant erbb2 comprenant des agents chimiothérapeutiques à base d'anthracycline |
CA2822283A1 (fr) * | 2010-12-23 | 2012-06-28 | Nestec S.A. | Selection de medicament pour traitement de cancer a l'aide de reseaux a base d'anticorps |
JP5766296B2 (ja) | 2010-12-23 | 2015-08-19 | エフ.ホフマン−ラ ロシュ アーゲーF. Hoffmann−La Roche Aktiengesellschaft | ポリペプチド−ポリヌクレオチド複合体、およびエフェクター成分の標的化された送達におけるその使用 |
WO2012099968A1 (fr) * | 2011-01-19 | 2012-07-26 | The Trustees Of The University Of Pennsylvania | Compositions et procédés de traitement de maladies associées à un cancer de la peau |
WO2012103341A1 (fr) * | 2011-01-27 | 2012-08-02 | Merrimack Pharmaceuticals, Inc. | Traitement de tumeurs solides à un stade avancé à l'aide d'anticorps anti-erbb3 |
WO2012112730A2 (fr) | 2011-02-15 | 2012-08-23 | Merrimack Pharmaceuticals, Inc. | Compositions et procédés pour délivrer un acide nucléique à une cellule |
CN103502271B (zh) | 2011-02-28 | 2016-10-26 | 霍夫曼-拉罗奇有限公司 | 抗原结合蛋白 |
RU2013141078A (ru) | 2011-02-28 | 2015-04-10 | Ф. Хоффманн-Ля Рош Аг | Одновалентные антигенсвязывающие белки |
JP6100704B2 (ja) | 2011-03-07 | 2017-03-22 | エフ・ホフマン−ラ・ロシュ・アクチェンゲゼルシャフト | 治療用抗体についてのインビボ試験の手段および方法 |
EA201300996A1 (ru) * | 2011-03-11 | 2014-01-30 | Мерримак Фармасьютикалс, Инк. | Использование ингибиторов рецепторов семейства egfr в лечении гормонорезистентного рака молочной железы |
SG192775A1 (en) | 2011-03-15 | 2013-09-30 | Merrimack Pharmaceuticals Inc | Overcoming resistance to erbb pathway inhibitors |
CN105884900A (zh) | 2011-04-19 | 2016-08-24 | 梅里麦克制药股份有限公司 | 单特异性和双特异性抗igf-1r和抗erbb3抗体 |
UA117218C2 (uk) | 2011-05-05 | 2018-07-10 | Мерк Патент Гмбх | Поліпептид, спрямований проти il-17a, il-17f та/або il17-a/f |
US20140234317A1 (en) * | 2011-05-06 | 2014-08-21 | Merrimack Pharmaceuticals, Inc. | Methods for preventing toxic drug-drug interactions in combination therapies comprising anti-erbb3 agents |
PT2707391T (pt) | 2011-05-13 | 2018-02-06 | Inserm Institut National De La Santa© Et De La Rech Ma©Dicale | Anticorpos contra her3 |
CN107903325B (zh) | 2011-05-16 | 2021-10-29 | 埃泰美德(香港)有限公司 | 多特异性fab融合蛋白及其使用方法 |
KR102101806B1 (ko) * | 2011-05-19 | 2020-04-20 | 인쎄름 (엥스띠뛰 나씨오날 드 라 쌍떼 에 드 라 흐쉐르슈 메디깔) | 항-인간-her3 항체 및 이의 용도 |
WO2012173867A1 (fr) * | 2011-06-16 | 2012-12-20 | Merrimack Pharmaceuticals, Inc. | Dosage et administration d'anticorps anti-erbb3 en combinaison avec des inhibiteurs de tyrosine kinase |
AU2012274461A1 (en) * | 2011-06-20 | 2014-01-16 | Kyowa Hakko Kirin Co., Ltd. | Anti-erbB3 antibody |
AU2012273361A1 (en) * | 2011-06-24 | 2013-03-21 | Merrimack Pharmaceuticals, Inc. | Dosage and administration of anti-ErbB3 antibodies in combination with paclitaxel |
KR20140063578A (ko) * | 2011-06-30 | 2014-05-27 | 메리맥 파마슈티컬즈, 인크. | 부인과 암들의 치료를 위해 파크리탁셀과 조합한 항-erbb3 항체들 |
CA2842860A1 (fr) * | 2011-07-28 | 2013-01-31 | Sea Lane Biotechnologies, Llc | Proteines se liant a sur dirigees contre erbb3 |
AU2012294326A1 (en) * | 2011-08-10 | 2013-03-21 | Merrimack Pharmaceuticals, Inc. | Treatment of advanced solid tumors using combination of anti-ErbB3 immunotherapy and selected chemotherapy |
EP2748197A2 (fr) | 2011-08-26 | 2014-07-02 | Merrimack Pharmaceuticals, Inc. | Anticorps bispécifiques à fc en tandem |
US9273143B2 (en) | 2011-09-30 | 2016-03-01 | Regeneron Pharmaceuticals, Inc. | Methods and compositions comprising a combination of an anti-ErbB3 antibody and an anti-EGFR antibody |
MX357391B (es) | 2011-09-30 | 2018-07-06 | Regeneron Pharma | Anticuerpos anti-erbb3 y usos de los mismos. |
US9828635B2 (en) * | 2011-10-06 | 2017-11-28 | Aveo Pharmaceuticals, Inc. | Predicting tumor response to anti-ERBB3 antibodies |
US9637543B2 (en) | 2011-11-09 | 2017-05-02 | The Uab Research Foundation | HER3 antibodies and uses thereof |
US9220775B2 (en) | 2011-11-23 | 2015-12-29 | Medimmune Llc | Binding molecules specific for HER3 and uses thereof |
EA036739B1 (ru) | 2011-12-05 | 2020-12-15 | Новартис Аг | Антитела к рецептору эпидермального фактора роста 3 (her3) |
EP2793940B1 (fr) | 2011-12-22 | 2018-11-14 | i2 Pharmaceuticals, Inc. | Protéines substitutives de liaison |
US9120870B2 (en) | 2011-12-30 | 2015-09-01 | Abbvie Inc. | Dual specific binding proteins directed against IL-13 and IL-17 |
NZ627878A (en) | 2012-01-13 | 2016-03-31 | Nippon Chemiphar Co | P2x4 receptor antagonist |
EP2812357B1 (fr) | 2012-02-10 | 2020-11-04 | F.Hoffmann-La Roche Ag | Anticorps et autres hétéromultimères monocaténaires |
EP2817335A1 (fr) * | 2012-02-22 | 2014-12-31 | U3 Pharma GmbH | Composition d'une protéine de liaison d'hb-egf et d'un inhibiteur de l'egfr |
AU2013201584A1 (en) * | 2012-03-12 | 2013-09-26 | Merrimack Pharmaceuticals, Inc. | Methods for treating pancreatic cancer using combination therapies comprising an anti-ErbB3 antibody |
WO2013148315A1 (fr) | 2012-03-27 | 2013-10-03 | Genentech, Inc. | Diagnostic et traitements concernant des inhibiteurs de her3 |
MX358728B (es) | 2012-05-02 | 2018-09-03 | Symphogen As | Composiciones de anticuerpos pan-receptor del factor de crecimiento epidermico humano (pan-her) humanizados. |
AU2013202947B2 (en) | 2012-06-13 | 2016-06-02 | Ipsen Biopharm Ltd. | Methods for treating pancreatic cancer using combination therapies comprising liposomal irinotecan |
US9717724B2 (en) | 2012-06-13 | 2017-08-01 | Ipsen Biopharm Ltd. | Methods for treating pancreatic cancer using combination therapies |
MX354862B (es) | 2012-06-27 | 2018-03-23 | Hoffmann La Roche | Método para la producción de entidades dirigidas altamente selectivas hechas a la medida y biespecíficas que contienen dos entidades de unión diferentes. |
CA2871882A1 (fr) | 2012-06-27 | 2014-01-03 | F. Hoffmann-La Roche Ag | Methode de fabrication de conjugues d'anticorps a region fc comprenant au moins une entite de liaison qui se lie specifiquement a une cible et leurs utilisations |
JP2015529236A (ja) | 2012-09-25 | 2015-10-05 | グレンマーク ファーマシューティカルズ, エセ.アー. | ヘテロ二量体免疫グロブリンの精製 |
KR102191655B1 (ko) | 2012-10-05 | 2020-12-16 | 애피바디 에이비 | Her3 결합 폴리펩티드 |
KR101820699B1 (ko) | 2012-11-01 | 2018-01-22 | 애브비 인코포레이티드 | 항-vegf/dll4 이원 가변 도메인 면역글로불린 및 이의 용도 |
MX2015005756A (es) | 2012-11-08 | 2015-09-16 | Hoffmann La Roche | Proteinas de unión a antígeno anti-her3/her4 de unión a la horquilla beta de her3 y a la horquilla beta de her4. |
MA38165A1 (fr) | 2012-11-08 | 2018-07-31 | Hoffmann La Roche | Protéines de liaison à l'antigène her3 se liant à l'épingle à cheveux beta de her3 |
SG11201504293WA (en) | 2012-12-03 | 2015-06-29 | Merrimack Pharmaceuticals Inc | Combination therapy for treating her2-positive cancers |
US9180185B2 (en) | 2013-01-11 | 2015-11-10 | Hoffman-La Roche Inc. | Combination therapy of anti-HER3 antibodies |
WO2014138449A1 (fr) | 2013-03-06 | 2014-09-12 | Merrimack Pharmaceuticals, Inc. | Anticorps bispécifiques anti-c-met à fc en tandem |
AU2014239903A1 (en) | 2013-03-14 | 2015-09-17 | Genentech, Inc. | Combinations of a MEK inhibitor compound with an HER3/EGFR inhibitor compound and methods of use |
WO2014144280A2 (fr) | 2013-03-15 | 2014-09-18 | Abbvie Inc. | Protéines de liaison spécifiques à domaines variables doubles dirigées contre il -1β et/ou il -17 |
US10239951B2 (en) * | 2013-05-08 | 2019-03-26 | Zymeworks Inc. | Bispecific HER2 and HER3 antigen binding constructs |
EP2821071A1 (fr) | 2013-07-04 | 2015-01-07 | Institut d'Investigació Biomèdica de Bellvitge (IDIBELL) | Composés pour le traitement du cancer du sein |
US11305012B2 (en) | 2013-09-24 | 2022-04-19 | Medimmune, Llc | Binding molecules specific for HER3 and uses thereof |
JP6422956B2 (ja) | 2013-10-11 | 2018-11-14 | エフ.ホフマン−ラ ロシュ アーゲーF. Hoffmann−La Roche Aktiengesellschaft | 多重特異性ドメイン交換共通可変軽鎖抗体 |
WO2015066543A1 (fr) | 2013-11-01 | 2015-05-07 | Board Of Regents, The University Of Texas System | Ciblage de her2 et her3 avec des anticorps bispécifiques dans des cellules cancéreuses |
JP6449876B2 (ja) | 2013-11-07 | 2019-01-09 | アンスティチュ ナショナル ドゥ ラ サンテ エ ドゥ ラ ルシェルシュ メディカル | ニューレグリンに対して非競合的でアロステリックな抗ヒトher3抗体及びその使用 |
WO2015100459A2 (fr) | 2013-12-27 | 2015-07-02 | Merrimack Pharmaceuticals, Inc. | Profils de biomarqueur pour prédire les résultats d'une thérapie cancéreuse utilisant des inhibiteurs d'erbb3 et/ou des chimiothérapies |
KR102127408B1 (ko) | 2014-01-29 | 2020-06-29 | 삼성전자주식회사 | 항 Her3 scFv 단편 및 이를 포함하는 항 c-Met/항 Her3 이중 특이 항체 |
WO2015130173A1 (fr) | 2014-02-28 | 2015-09-03 | Merus B.V. | Anticorps qui se lie à erbb-2 et erbb-3 |
CA2941030A1 (fr) | 2014-02-28 | 2015-09-03 | Merus N.V. | Anticorps qui se lient a l'egfr et a l'erbb3 |
PE20161211A1 (es) | 2014-03-21 | 2016-11-27 | Abbvie Inc | Anticuerpos y conjugados de anticuerpo y farmaco anti-egfr |
KR102359214B1 (ko) | 2014-04-04 | 2022-02-07 | 델 마 파마슈티컬스 | 폐의 비소세포 암종 및 난소암을 치료하기 위한 디안하이드로갈락티톨 및 이의 유사체 또는 유도체 |
SG11201608309PA (en) | 2014-04-10 | 2016-11-29 | Daiichi Sankyo Co Ltd | Anti-her3 antibody-drug conjugate |
WO2015157634A1 (fr) | 2014-04-11 | 2015-10-15 | Kolltan Pharmaceuticals, Inc. | Anticorps anti-erbb et leurs méthodes d'utilisation |
FR3020063A1 (fr) | 2014-04-16 | 2015-10-23 | Gamamabs Pharma | Anticorps humain anti-her4 |
CA2944895A1 (fr) * | 2014-05-14 | 2015-11-19 | F. Hoffmann-La Roche Ag | Anticorps anti-her3 se liant a l'epingle a cheveux beta de her3 |
US20160045596A1 (en) | 2014-08-05 | 2016-02-18 | Merrimack Pharmaceuticals, Inc. | Combination therapies for treating her2-positive cancers that are resistant to her2-targeted therapies |
CN107001482B (zh) | 2014-12-03 | 2021-06-15 | 豪夫迈·罗氏有限公司 | 多特异性抗体 |
US10093733B2 (en) | 2014-12-11 | 2018-10-09 | Abbvie Inc. | LRP-8 binding dual variable domain immunoglobulin proteins |
JP2018513155A (ja) * | 2015-04-17 | 2018-05-24 | メリマック ファーマシューティカルズ インコーポレーティッド | セリバンツマブを用いた併用療法 |
EP3091033A1 (fr) | 2015-05-06 | 2016-11-09 | Gamamabs Pharma | Anticorps anti-her3 humains et leurs utilisations |
US11318131B2 (en) | 2015-05-18 | 2022-05-03 | Ipsen Biopharm Ltd. | Nanoliposomal irinotecan for use in treating small cell lung cancer |
AU2016271138A1 (en) | 2015-05-29 | 2017-12-07 | Merrimack Pharmaceuticals, Inc. | Combination cancer therapies |
US10184006B2 (en) | 2015-06-04 | 2019-01-22 | Merrimack Pharmaceuticals, Inc. | Biomarkers for predicting outcomes of cancer therapy with ErbB3 inhibitors |
TW201710286A (zh) | 2015-06-15 | 2017-03-16 | 艾伯維有限公司 | 抗vegf、pdgf及/或其受體之結合蛋白 |
IL290959B2 (en) | 2015-06-29 | 2023-04-01 | Daiichi Sankyo Co Ltd | Preparations containing antibody-drug conjugates and methods for their production |
TW201716439A (zh) | 2015-07-20 | 2017-05-16 | 美國禮來大藥廠 | Her3抗體 |
CA2992789A1 (fr) | 2015-08-20 | 2017-02-23 | Ipsen Biopharm Ltd. | Traitement combine utilisant l'irinotecan liposomal et un inhibiteur de parp pour un traitement anticancereux |
KR102714060B1 (ko) | 2015-08-21 | 2024-10-08 | 입센 바이오팜 리미티드 | 리포솜 이리노테칸 및 옥살리플라틴을 포함하는 병용 치료를 이용하여 전이성 췌장암을 치료하는 방법 |
WO2017035482A1 (fr) * | 2015-08-27 | 2017-03-02 | Merrimack Pharmaceuticals, Inc | Polythérapies pour le traitement de cancers positifs à l'héréguline |
EP3352859B1 (fr) | 2015-09-24 | 2020-09-23 | Expression Pathology, Inc. | Quantification de la protéine met pour le traitement du cancer |
MA42991A (fr) | 2015-10-16 | 2018-08-22 | Ipsen Biopharm Ltd | Stabilisation de compositions pharmaceutiques de camptothécine |
JP7296728B2 (ja) | 2015-10-23 | 2023-06-23 | メルス ナムローゼ フェンノートシャップ | 癌の成長を抑制する結合分子 |
US20180271998A1 (en) | 2015-12-04 | 2018-09-27 | Merrimack Pharmaceuticals, Inc. | Disulfide-stabilized fabs |
KR101746152B1 (ko) | 2015-12-07 | 2017-06-13 | 주식회사 이수앱지스 | ErbB3에 특이적으로 결합하는 항체 및 그의 용도 |
CN106854244B (zh) * | 2015-12-09 | 2020-05-22 | 南京英瀚斯生物科技有限公司 | 一种针对her3的纳米抗体及其临床应用 |
JP2018536682A (ja) | 2015-12-11 | 2018-12-13 | リジェネロン・ファーマシューティカルズ・インコーポレイテッドRegeneron Pharmaceuticals, Inc. | Egfr及び/またはerbb3遮断に耐性のある腫瘍の成長を低減または防止するための方法 |
SG10201601719RA (en) | 2016-03-04 | 2017-10-30 | Agency Science Tech & Res | Anti-LAG-3 Antibodies |
CA3017776A1 (fr) | 2016-03-15 | 2017-09-21 | Generon (Shanghai) Corporation Ltd. | Proteines de fusion a fab multispecifiques et leur utilisation |
WO2017160990A1 (fr) | 2016-03-15 | 2017-09-21 | Merrimack Pharmaceuticals, Inc. | Méthodes de traitement du cancer du sein er+, her2-hrg+ à l'aide de traitements d'association comportant un anticorps anti-erbb3 |
SG10201603721TA (en) | 2016-05-10 | 2017-12-28 | Agency Science Tech & Res | Anti-CTLA-4 Antibodies |
AU2017277534A1 (en) | 2016-06-08 | 2019-01-03 | Abbvie Inc. | Anti-EGFR antibody drug conjugates |
JP2019526529A (ja) | 2016-06-08 | 2019-09-19 | アッヴィ・インコーポレイテッド | 抗b7−h3抗体及び抗体薬物コンジュゲート |
AU2017277914A1 (en) | 2016-06-08 | 2019-01-03 | Abbvie Inc. | Anti-CD98 antibodies and antibody drug conjugates |
JP6751165B2 (ja) | 2016-06-08 | 2020-09-02 | アッヴィ・インコーポレイテッド | 抗b7−h3抗体及び抗体薬物コンジュゲート |
EP3469000A1 (fr) | 2016-06-08 | 2019-04-17 | AbbVie Inc. | Anticorps anti-b7-h3 et conjugués anticorps-médicaments |
CA3027173A1 (fr) | 2016-06-08 | 2017-12-14 | Abbvie Inc. | Conjugue medicament-anticorps anti-egfr |
MX2019004783A (es) | 2016-11-02 | 2019-08-12 | Ipsen Biopharm Ltd | Tratamiento de cancer gastrico usando terapias de combinacion que comprenden irinotecan liposomico oxaliplatino, 5-fluoruracilo (y leucovorina). |
TW201828993A (zh) | 2016-12-12 | 2018-08-16 | 日商第一三共股份有限公司 | 抗體-藥物結合物與免疫檢查點抑制劑之組合 |
EP3555120A1 (fr) | 2016-12-19 | 2019-10-23 | Abcam Plc | Protéines de liaison monovalentes et divalentes |
TWI780104B (zh) | 2017-01-17 | 2022-10-11 | 日商第一三共股份有限公司 | 抗gpr20抗體及抗gpr20抗體-藥物結合物、以及其製造方法及用途 |
WO2018159582A1 (fr) | 2017-02-28 | 2018-09-07 | 学校法人近畿大学 | Méthode de traitement du cancer du poumon non à petites cellules résistant à l'egfr-tki par administration d'un conjugué anticorps anti-her3-médicament |
CN110650752A (zh) | 2017-03-31 | 2020-01-03 | 美勒斯公司 | 用于治疗具有NRG1融合基因的细胞的ErbB-2和ErbB3结合双特异性抗体 |
JP7304815B2 (ja) | 2017-03-31 | 2023-07-07 | メルス ナムローゼ フェンノートシャップ | Erbb-2、erbb-2/erbb-3陽性腫瘍を有する個体の処置のための、erb-2及びerbb-3の細胞外部分上のエピトープに結合する抗原結合部位を含むerbb-2標的化剤及び二重特異性抗体 |
CA3064697A1 (fr) | 2017-04-19 | 2018-10-25 | Bluefin Biomedicine, Inc. | Anticorps anti-vtcn1 et conjugues anticorps-medicament |
WO2018204153A1 (fr) * | 2017-05-02 | 2018-11-08 | Venomyx, Inc. | Composition et procédés de traitement de l'envenimation par un serpent |
TWI794230B (zh) | 2017-05-15 | 2023-03-01 | 日商第一三共股份有限公司 | 抗cdh6抗體及抗cdh6抗體-藥物結合物、以及其製造方法 |
US11773170B2 (en) | 2017-08-09 | 2023-10-03 | Merus N.V. | Antibodies that bind EGFR and cMET |
US20210128741A1 (en) | 2017-08-23 | 2021-05-06 | Daiichi Sankyo Company, Limited | Antibody-drug conjugate preparation and lyophilization for same |
CA3073924C (fr) | 2017-08-31 | 2023-10-17 | Daiichi Sankyo Company, Limited | Procede ameliore de production d'un conjugue anticorps-medicament |
EP3677568A4 (fr) | 2017-08-31 | 2021-05-12 | Daiichi Sankyo Company, Limited | Nouveau procédé de production d'un conjugué anticorps-médicament |
WO2019118318A1 (fr) | 2017-12-12 | 2019-06-20 | Calico Biolabs, Inc. | Anticorps recombinant comprenant une chaîne lourde génétiquement fusionnée à une signature peptidique et ses utilisations |
EP3794041B1 (fr) | 2018-05-18 | 2023-07-12 | Glycotope GmbH | Anticorps anti-muc1 |
BR112021001194A2 (pt) | 2018-07-25 | 2021-04-27 | Daiichi Sankyo Company, Limited | métodos para produzir um conjugado anticorpo-fármaco e para produzir uma composição farmacêutica |
JP7406488B2 (ja) | 2018-07-27 | 2023-12-27 | 第一三共株式会社 | 抗体-薬物コンジュゲートの薬物部位を認識する蛋白質 |
TWI822822B (zh) | 2018-07-31 | 2023-11-21 | 日商第一三共股份有限公司 | 抗體-藥物結合物之用途 |
US20210290775A1 (en) | 2018-08-06 | 2021-09-23 | Daiichi Sankyo Company, Limited | Combination of antibody-drug conjugate and tubulin inhibitor |
JP7481255B2 (ja) | 2018-08-23 | 2024-05-10 | 第一三共株式会社 | 抗体薬物複合体の感受性マーカー |
TW202024133A (zh) | 2018-09-20 | 2020-07-01 | 日商第一三共股份有限公司 | 利用投予抗her3抗體-藥物結合物之her3突變癌之治療 |
AU2019396895A1 (en) | 2018-12-11 | 2021-07-08 | Daiichi Sankyo Company, Limited | Combination of antibody-drug conjugate with PARP inhibitor |
JPWO2020130125A1 (ja) | 2018-12-21 | 2021-11-04 | 第一三共株式会社 | 抗体−薬物コンジュゲートとキナーゼ阻害剤の組み合わせ |
WO2022078490A1 (fr) * | 2020-10-15 | 2022-04-21 | 上海翰森生物医药科技有限公司 | Anticorps anti-erbb3 ou fragment de liaison à l'antigène de celui-ci et utilisation médicale associée |
IL302812A (en) | 2020-11-11 | 2023-07-01 | Daiichi Sankyo Co Ltd | Antibody-drug conjugate combinations with anti-SIRP alpha antibody |
UY39610A (es) | 2021-01-20 | 2022-08-31 | Abbvie Inc | Conjugados anticuerpo-fármaco anti-egfr |
US20220288204A1 (en) * | 2021-03-11 | 2022-09-15 | Elevation Oncology, Inc. | Dosage and administration of anti-erbb3 (her3) monoclonal antibodies to treat tumors associated with neuregulin 1 (nrg1) gene fusions |
WO2023198138A1 (fr) * | 2022-04-13 | 2023-10-19 | 上海翰森生物医药科技有限公司 | Anticorps ou fragment de liaison à l'antigène de celui-ci et son utilisation médicale |
WO2023209591A1 (fr) | 2022-04-27 | 2023-11-02 | Daiichi Sankyo Company, Limited | Combinaison d'un conjugué anticorps-médicament avec un inhibiteur de l'ezh1 et/ou de l'ezh2 |
WO2023218378A1 (fr) | 2022-05-11 | 2023-11-16 | Daiichi Sankyo Company, Limited | Association combinant un anticorps spécifique d'un antigène tumoral et un inhibiteur de cd47 |
WO2024127366A1 (fr) | 2022-12-16 | 2024-06-20 | Pheon Therapeutics Ltd | Anticorps dirigés contre la protéine 1 contenant le domaine cub (cdcp1) et leurs utilisations |
Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1997035885A1 (fr) * | 1996-03-27 | 1997-10-02 | Genentech, Inc. | ANTICORPS DE LA PROTEINE ErbB3 |
EP1283053A1 (fr) * | 2001-08-09 | 2003-02-12 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | Inhibiteurs de l'activité de HER3 |
WO2006017538A2 (fr) * | 2004-08-03 | 2006-02-16 | Dyax Corp. | Proteines de liaison a la proteine hk1 |
WO2006020706A2 (fr) * | 2004-08-12 | 2006-02-23 | Dyax Corp. | Proteines de liaison au complexe tie |
WO2006091209A2 (fr) * | 2005-02-23 | 2006-08-31 | Merrimack Pharmaceuticals, Inc. | Agents de liaison bispecifiques utilises pour moduler une activite biologique |
Family Cites Families (123)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4475196A (en) | 1981-03-06 | 1984-10-02 | Zor Clair G | Instrument for locating faults in aircraft passenger reading light and attendant call control system |
US4447233A (en) | 1981-04-10 | 1984-05-08 | Parker-Hannifin Corporation | Medication infusion pump |
US4439196A (en) | 1982-03-18 | 1984-03-27 | Merck & Co., Inc. | Osmotic drug delivery system |
US4522811A (en) | 1982-07-08 | 1985-06-11 | Syntex (U.S.A.) Inc. | Serial injection of muramyldipeptides and liposomes enhances the anti-infective activity of muramyldipeptides |
US4447224A (en) | 1982-09-20 | 1984-05-08 | Infusaid Corporation | Variable flow implantable infusion apparatus |
US4487603A (en) | 1982-11-26 | 1984-12-11 | Cordis Corporation | Implantable microinfusion pump system |
US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
US4486194A (en) | 1983-06-08 | 1984-12-04 | James Ferrara | Therapeutic device for administering medicaments through the skin |
US4596556A (en) | 1985-03-25 | 1986-06-24 | Bioject, Inc. | Hypodermic injection apparatus |
US5374548A (en) | 1986-05-02 | 1994-12-20 | Genentech, Inc. | Methods and compositions for the attachment of proteins to liposomes using a glycophospholipid anchor |
MX9203291A (es) | 1985-06-26 | 1992-08-01 | Liposome Co Inc | Metodo para acoplamiento de liposomas. |
US4790824A (en) | 1987-06-19 | 1988-12-13 | Bioject, Inc. | Non-invasive hypodermic injection device |
US4941880A (en) | 1987-06-19 | 1990-07-17 | Bioject, Inc. | Pre-filled ampule and non-invasive hypodermic injection device assembly |
US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
US5108921A (en) | 1989-04-03 | 1992-04-28 | Purdue Research Foundation | Method for enhanced transmembrane transport of exogenous molecules |
US5312335A (en) | 1989-11-09 | 1994-05-17 | Bioject Inc. | Needleless hypodermic injection device |
US5064413A (en) | 1989-11-09 | 1991-11-12 | Bioject, Inc. | Needleless hypodermic injection device |
US5183884A (en) | 1989-12-01 | 1993-02-02 | United States Of America | Dna segment encoding a gene for a receptor related to the epidermal growth factor receptor |
WO1991010741A1 (fr) | 1990-01-12 | 1991-07-25 | Cell Genesys, Inc. | Generation d'anticorps xenogeniques |
US6657103B1 (en) | 1990-01-12 | 2003-12-02 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
US6673986B1 (en) | 1990-01-12 | 2004-01-06 | Abgenix, Inc. | Generation of xenogeneic antibodies |
US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
US6172197B1 (en) | 1991-07-10 | 2001-01-09 | Medical Research Council | Methods for producing members of specific binding pairs |
GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
US5789650A (en) | 1990-08-29 | 1998-08-04 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
US6300129B1 (en) | 1990-08-29 | 2001-10-09 | Genpharm International | Transgenic non-human animals for producing heterologous antibodies |
US5877397A (en) | 1990-08-29 | 1999-03-02 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
US6255458B1 (en) | 1990-08-29 | 2001-07-03 | Genpharm International | High affinity human antibodies and human antibodies against digoxin |
US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
CA2089661C (fr) | 1990-08-29 | 2007-04-03 | Nils Lonberg | Animaux transgeniques non humains capables de produire des anticorps heterologues |
US5874299A (en) | 1990-08-29 | 1999-02-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
US5344760A (en) | 1991-06-03 | 1994-09-06 | Ciba Corning Diagnostics Corp. | Method of cancer detection |
WO1993011236A1 (fr) | 1991-12-02 | 1993-06-10 | Medical Research Council | Production d'anticorps anti-auto-antigenes a partir de repertoires de segments d'anticorps affiches sur phage |
CA2124967C (fr) | 1991-12-17 | 2008-04-08 | Nils Lonberg | Animaux transgeniques non humains capables de produire des anticorps heterologues |
US5383851A (en) | 1992-07-24 | 1995-01-24 | Bioject Inc. | Needleless hypodermic injection device |
DE69329503T2 (de) | 1992-11-13 | 2001-05-03 | Idec Pharma Corp | Therapeutische Verwendung von chimerischen und markierten Antikörpern, die gegen ein Differenzierung-Antigen gerichtet sind, dessen Expression auf menschliche B Lymphozyt beschränkt ist, für die Behandlung von B-Zell-Lymphoma |
AU6819494A (en) | 1993-04-26 | 1994-11-21 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
US6983227B1 (en) | 1995-01-17 | 2006-01-03 | Intertech Ventures, Ltd. | Virtual models of complex systems |
US5968511A (en) | 1996-03-27 | 1999-10-19 | Genentech, Inc. | ErbB3 antibodies |
CA2258721C (fr) | 1996-07-12 | 2014-09-09 | Genentech, Inc. | Adhesines heteromultimeres chimeriques |
US6255455B1 (en) * | 1996-10-11 | 2001-07-03 | The Trustees Of The University Of Pennsylvania | Rh(D)-binding proteins and magnetically activated cell sorting method for production thereof |
US20020002276A1 (en) | 1997-02-10 | 2002-01-03 | Genentech, Inc. | Chimeric heteromultimer adhesins |
US6040498A (en) | 1998-08-11 | 2000-03-21 | North Caroline State University | Genetically engineered duckweed |
US6417168B1 (en) | 1998-03-04 | 2002-07-09 | The Trustees Of The University Of Pennsylvania | Compositions and methods of treating tumors |
GB2336695A (en) | 1998-04-20 | 1999-10-27 | Teamware Group Oy | Modelling a work process |
IL139707A0 (en) | 1998-05-15 | 2002-02-10 | Imclone Systems Inc | Treatment of human tumors with radiation and inhibitors of growth factor receptor tyrosine kinases |
AUPQ105799A0 (en) | 1999-06-18 | 1999-07-08 | Victor Chang Cardiac Research Institute, The | Cell growth inhibition |
AU784012B2 (en) | 1999-08-24 | 2006-01-12 | E. R. Squibb & Sons, L.L.C. | Human CTLA-4 antibodies and their uses |
TR200200472T2 (tr) | 1999-08-27 | 2002-06-21 | Genentech, Inc. | Anti-Erb B2 antikorları ile tedavi için dozajlar |
US7097840B2 (en) | 2000-03-16 | 2006-08-29 | Genentech, Inc. | Methods of treatment using anti-ErbB antibody-maytansinoid conjugates |
EP2330219A3 (fr) | 2000-04-14 | 2011-11-23 | Metabolon, Inc. | Procédé de découverte de médicament, traitement de maladie et diagnostic utilisant les métabolomiques. |
US20020064785A1 (en) | 2000-05-19 | 2002-05-30 | Genentech Inc. | Gene detection assay for improving the likelihood of an effective response to an ErbB antagonist cancer therapy |
CA2417415C (fr) | 2000-07-31 | 2012-10-09 | Biolex, Inc. | Expression de polypeptides biologiquement actifs dans une lenticule mineure |
US20020119148A1 (en) | 2000-09-01 | 2002-08-29 | Gerritsen Mary E. | ErbB4 antagonists |
US6871171B1 (en) | 2000-10-19 | 2005-03-22 | Optimata Ltd. | System and methods for optimized drug delivery and progression of diseased and normal cells |
WO2002043478A2 (fr) | 2000-11-30 | 2002-06-06 | Medarex, Inc. | Rongeurs transgeniques et transchromosomiques pour la fabrication d'anticorps humains |
EP1228766A1 (fr) | 2001-01-31 | 2002-08-07 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | Phosphorylation de PYK2 par HER3 induit l'invasion de tumeurs |
US7638302B2 (en) | 2001-05-31 | 2009-12-29 | Tumor Biology Investment Group, Inc. | Soluble ErbB3 receptor isoforms |
WO2003011897A1 (fr) | 2001-07-27 | 2003-02-13 | The Regents Of The University Of California | Modulation de l'hereguline et de l'interaction du recepteur her3 |
JP2005508887A (ja) | 2001-08-03 | 2005-04-07 | コモンウェルス サイエンティフィック アンド インダストリアル リサーチ オーガニゼイション | Egf受容体の結晶構造に基づいたスクリーニング方法 |
US7662374B2 (en) | 2001-08-03 | 2010-02-16 | The Trustees Of The University Of Pennsylvania | Monoclonal antibodies to activated erbB family members and methods of use thereof |
US20050004018A1 (en) | 2001-10-19 | 2005-01-06 | Jose Jimeno | Use of antitumoral compound in cancer therapy |
US7415359B2 (en) | 2001-11-02 | 2008-08-19 | Gene Network Sciences, Inc. | Methods and systems for the identification of components of mammalian biochemical networks as targets for therapeutic agents |
CA2480099C (fr) | 2002-03-26 | 2019-01-08 | Zensun (Shanghai) Sci-Tech. Ltd. | Procedes fondes sur l'utilisation de erbb3 et compositions associees de traitement des neoplasmes |
US7332580B2 (en) | 2002-04-05 | 2008-02-19 | The Regents Of The University Of California | Bispecific single chain Fv antibody molecules and methods of use thereof |
US20040248151A1 (en) | 2002-04-05 | 2004-12-09 | Ventana Medical Systems, Inc. | Method for predicting the response to HER2-directed therapy |
US20040229380A1 (en) | 2002-05-21 | 2004-11-18 | Po-Ying Chan-Hui | ErbB heterodimers as biomarkers |
WO2004000102A2 (fr) | 2002-06-19 | 2003-12-31 | Abgenix, Inc. | Procede servant a predire une reponse a une therapie dirigee vers le recepteur du facteur de croissance epidermique |
CN1678634A (zh) * | 2002-06-28 | 2005-10-05 | 多曼蒂斯有限公司 | 免疫球蛋白单个变体抗原结合区及其特异性构建体 |
BRPI0408950A (pt) | 2003-04-01 | 2006-03-28 | Monogram Biosciences Inc | método para determinar a situação de doença de um paciente, e, método para selecionar um paciente para tratamento de um cáncer com um ou mais medicamentos de ação dimérica |
WO2005014618A2 (fr) | 2003-08-08 | 2005-02-17 | Immunomedics, Inc. | Anticorps bispecifiques pour induire l'apoptose de cellules tumorales et malades |
EP1664716A4 (fr) | 2003-08-15 | 2008-08-13 | Smithkline Beecham Corp | Biomarqueurs contre le cancer |
US8554486B2 (en) | 2004-02-20 | 2013-10-08 | The Mathworks, Inc. | Method, computer program product, and apparatus for selective memory restoration of a simulation |
DK2447375T3 (da) | 2004-03-31 | 2019-07-29 | Massachusetts Gen Hospital | Fremgangsmåde til bestemmelse af responsiviteten af en tumor på behandlinger med den epidermale vækstfaktor-receptor som mål |
CN1997382A (zh) | 2004-05-05 | 2007-07-11 | 梅里麦克制药股份有限公司 | 调节生物活性的双特异性结合剂 |
WO2005117553A2 (fr) | 2004-05-27 | 2005-12-15 | The Regents Of The University Of Colorado | Methodes de prediction d'un avantage clinique relativement a des inhibiteurs du recepteur de facteur de croissance epidermique pour des cancereux |
WO2005121380A1 (fr) | 2004-06-04 | 2005-12-22 | Smithkline Beecham Corporation | Biomarqueurs predictifs utilises dans le traitement du cancer |
ATE508753T1 (de) | 2004-08-06 | 2011-05-15 | Genentech Inc | Assays und verfahren unter verwendung von biomarkern |
US20060136139A1 (en) | 2004-10-12 | 2006-06-22 | Elcock Adrian H | Rapid computational identification of targets |
WO2006044748A2 (fr) | 2004-10-15 | 2006-04-27 | Monogram Biosciences, Inc. | Predicteurs de reponse pour medicaments specifiques de la voie erbb |
US20060204505A1 (en) | 2005-03-08 | 2006-09-14 | Sliwkowski Mark X | Methods for identifying tumors responsive to treatment with HER dimerization inhibitors (HDIs) |
US20090061422A1 (en) | 2005-04-19 | 2009-03-05 | Linke Steven P | Diagnostic markers of breast cancer treatment and progression and methods of use thereof |
US20090298061A1 (en) | 2005-07-29 | 2009-12-03 | Siemens Healthcare Diagnostics Inc. | Diagnostic Methods for the Prediction of Therapeutic Success, Recurrence Free and Overall Survival in Cancer Therapy |
WO2007041502A2 (fr) | 2005-09-30 | 2007-04-12 | Monogram Biosciences | Procedes pour la determination de la sensibilite a la therapie cancereuse |
AU2005337051A1 (en) | 2005-10-05 | 2007-04-12 | Astrazeneca Uk Limited | Method to predict or monitor the response of a patient to an ErbB receptor drug |
AR056857A1 (es) * | 2005-12-30 | 2007-10-24 | U3 Pharma Ag | Anticuerpos dirigidos hacia her-3 (receptor del factor de crecimiento epidérmico humano-3) y sus usos |
WO2007109571A2 (fr) | 2006-03-17 | 2007-09-27 | Prometheus Laboratories, Inc. | Procédés de prédiction et de suivi de la thérapie par l'inhibiteur de la tyrosine kinase |
EP2049568A2 (fr) | 2006-04-07 | 2009-04-22 | Københavns Universitet | Fragments peptidiques dérivés du récepteur erbb |
US8367351B2 (en) | 2006-05-05 | 2013-02-05 | Historx, Inc. | Methods for determining signal transduction activity in tumors |
JP2009544007A (ja) | 2006-07-13 | 2009-12-10 | イェール・ユニバーシティー | バイオマーカーの細胞内局在性に基づいて癌予後を行う方法 |
US20100178651A1 (en) | 2006-11-03 | 2010-07-15 | Christos Hatzis | Bifunctional Predictors of Cancer Treatment Sensitivity and Resistance |
US20100047829A1 (en) | 2006-11-28 | 2010-02-25 | U3 Pharma Gmbh | Activated her3 as a marker for predicting therapeutic efficacy |
US7825127B2 (en) | 2006-12-28 | 2010-11-02 | Takeda Pharmaceutical Company, Limited | Method for treating cancer |
EP2647388A1 (fr) * | 2007-02-16 | 2013-10-09 | Merrimack Pharmaceuticals, Inc. | Anticorps dirigés contre l'ERBB3 et leurs utilisations |
SI2132573T1 (sl) | 2007-03-02 | 2014-07-31 | Genentech, Inc. | Napovedovanje odziva na inhibitor dimerizacije HER na osnovi nizke ekspresije HER3 |
JP5926487B2 (ja) | 2007-04-13 | 2016-05-25 | デイナ ファーバー キャンサー インスティチュート,インコーポレイテッド | ErbB療法に耐性である癌を治療するための方法 |
MX2009012271A (es) | 2007-05-11 | 2010-02-04 | Enzon Pharmaceuticals Inc | Compuestos antagonistas de acido ribonucleico para la modulacion de her3. |
PE20120015A1 (es) | 2008-08-15 | 2012-01-26 | Merrimack Pharmaceuticals Inc | Metodos y sistemas para predecir la respuesta de las celulas tumorales a un agente terapeutico |
US8927694B2 (en) | 2008-11-18 | 2015-01-06 | Merrimack Pharmaceuticals, Inc. | Human serum albumin linkers and conjugates thereof |
CA2771744A1 (fr) | 2009-08-21 | 2011-02-24 | Merrimack Pharmaceuticals, Inc. | Anticorps contre l'ectodomaine de erbb3 et leurs utilisations |
DK2544680T3 (en) * | 2010-03-11 | 2015-04-27 | Merrimack Pharmaceuticals Inc | USE OF ErbB3 INHIBITORS IN TREATMENT OF TRIPLE-NEGATIVE BREAST CANCER |
US8877687B2 (en) | 2010-04-26 | 2014-11-04 | Merrimack Pharmaceuticals | Assays for anti-drug antibodies in the presence of abundant endogenous protein counterpart of the drug |
UY33498A (es) | 2010-07-09 | 2013-01-03 | Sanofi Aventis | Combinaciones de inhibidores de quinasas para el tratamiento de cancer |
BR112013012213A2 (pt) * | 2010-11-17 | 2020-09-01 | Chugai Seiyaku Kabushiki Kaisha | moléculas de ligação a antígeno mul tlespecíficas tendo função alternativa à função dos fatores viii, ix e x de coagulação sanguínea, e anticorpo bies- 5 pecífico, seus usos na prevenção ou tratamento de hemorragia, ácido nucleico, vetor, célula, método para produzir as referidas moléculas de ligação, composição farmacêutica e kit |
AU2011341337A1 (en) | 2010-12-10 | 2013-06-13 | Merrimack Pharmaceuticals, Inc. | Dosage and administration of bispecific scFv conjugates |
WO2012116317A2 (fr) | 2011-02-24 | 2012-08-30 | Merrimack Pharmaceuticals, Inc. | Polythérapies comprenant des agents anti-erbb3 |
EA201300996A1 (ru) | 2011-03-11 | 2014-01-30 | Мерримак Фармасьютикалс, Инк. | Использование ингибиторов рецепторов семейства egfr в лечении гормонорезистентного рака молочной железы |
SG192775A1 (en) | 2011-03-15 | 2013-09-30 | Merrimack Pharmaceuticals Inc | Overcoming resistance to erbb pathway inhibitors |
CN105884900A (zh) | 2011-04-19 | 2016-08-24 | 梅里麦克制药股份有限公司 | 单特异性和双特异性抗igf-1r和抗erbb3抗体 |
US20140234317A1 (en) | 2011-05-06 | 2014-08-21 | Merrimack Pharmaceuticals, Inc. | Methods for preventing toxic drug-drug interactions in combination therapies comprising anti-erbb3 agents |
AU2012273361A1 (en) | 2011-06-24 | 2013-03-21 | Merrimack Pharmaceuticals, Inc. | Dosage and administration of anti-ErbB3 antibodies in combination with paclitaxel |
KR20140063578A (ko) | 2011-06-30 | 2014-05-27 | 메리맥 파마슈티컬즈, 인크. | 부인과 암들의 치료를 위해 파크리탁셀과 조합한 항-erbb3 항체들 |
US8790651B2 (en) * | 2011-07-21 | 2014-07-29 | Zoetis Llc | Interleukin-31 monoclonal antibody |
US20150202287A1 (en) | 2012-08-30 | 2015-07-23 | Merrimack Pharmaceuticals, Inc. | Combination therapies comprising anti-erbb3 agents |
WO2015100459A2 (fr) | 2013-12-27 | 2015-07-02 | Merrimack Pharmaceuticals, Inc. | Profils de biomarqueur pour prédire les résultats d'une thérapie cancéreuse utilisant des inhibiteurs d'erbb3 et/ou des chimiothérapies |
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Patent Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1997035885A1 (fr) * | 1996-03-27 | 1997-10-02 | Genentech, Inc. | ANTICORPS DE LA PROTEINE ErbB3 |
EP1283053A1 (fr) * | 2001-08-09 | 2003-02-12 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | Inhibiteurs de l'activité de HER3 |
WO2006017538A2 (fr) * | 2004-08-03 | 2006-02-16 | Dyax Corp. | Proteines de liaison a la proteine hk1 |
WO2006020706A2 (fr) * | 2004-08-12 | 2006-02-23 | Dyax Corp. | Proteines de liaison au complexe tie |
WO2006091209A2 (fr) * | 2005-02-23 | 2006-08-31 | Merrimack Pharmaceuticals, Inc. | Agents de liaison bispecifiques utilises pour moduler une activite biologique |
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